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Entry version 197 (02 Jun 2021)
Sequence version 2 (18 Oct 2001)
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Protein

Protective antigen

Gene

pagA

Organism
Bacillus anthracis
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Protective antigen constitutes one of the three proteins composing the anthrax toxin; it mediates attachment to host cells and translocation of edema factor (EF) and lethal factor (LF) into the host cytoplasm (PubMed:11700562, PubMed:14507921, PubMed:15243628, PubMed:15326297).

PA associated with LF forms the lethal toxin (LeTx) and causes death when injected; PA associated with EF forms the edema toxin (EdTx) and produces edema (PubMed:1651334).

PA induces immunity to infection with anthrax (PubMed:11544370).

1 Publication5 Publications

Mediates the attachment to host cells by binding host cell receptors ANTXR1 and ANTXR2 (PubMed:11700562, PubMed:14507921, PubMed:15243628, PubMed:15326297).

Following host cell surface attachment, PA is cleaved by FURIN to generate the PA-63 (Protective antigen PA-63) form, which constitutes the mature form of the protein that oligomerizes and forms a pore to translocate the enzymatic toxin components edema factor (EF) and lethal factor (LF) into the host cytosol (PubMed:11700562, PubMed:15243628, PubMed:15326297).

4 Publications

Mature form that oligomerizes and forms a pore to translocate the enzymatic toxin components edema factor (EF) and lethal factor (LF) into the host cytosol (PubMed:15243628, PubMed:15326297).

Following attachment to host cell receptors and cleavage by FURIN, homooligomerizes to form ring-shaped oligomers that are in a pre-pore conformation, and associates with EF and LF (PubMed:10085027, PubMed:12117959, PubMed:15313199).

Toxin-leaded complexes are then endocytosed in a clathrin-dependent process, followed by a conformational change of oligomerized PA-63 from the pre-pore to pore state, which is triggered by the low pH in the endosome (PubMed:10085027, PubMed:12551953, PubMed:20221438, PubMed:15326297).

Once active, the pore mediates unfolding of EF and LF, which pass through the pore and translocate into the host cytosol (PubMed:16051798, PubMed:21037566, PubMed:32047164, PubMed:32810181, PubMed:32521227).

12 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi206Calcium 1Combined sources6 Publications1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei207Alpha-clamp1 Publication1
Metal bindingi208Calcium 1Combined sources6 Publications1
Metal bindingi208Calcium 2Combined sources6 Publications1
Metal bindingi210Calcium 1Combined sources6 Publications1
Metal bindingi210Calcium 2Combined sources6 Publications1
Metal bindingi212Calcium 1; via carbonyl oxygenCombined sources6 Publications1
Sitei216Alpha-clamp1 Publication1
Metal bindingi217Calcium 1Combined sources6 Publications1
Metal bindingi217Calcium 2Combined sources4 Publications1
Metal bindingi251Calcium 2; via carbonyl oxygenCombined sources5 Publications1
Metal bindingi254Calcium 2; via carbonyl oxygenCombined sources5 Publications1
Metal bindingi264Calcium 2Combined sources4 Publications1
Sitei265Alpha-clamp1 Publication1
Sitei456Phi-clamp2 Publications1
Sitei493Alpha-clamp1 Publication1
Sitei712Essential for binding to cell receptor1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionToxin
Biological processVirulence
LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-5210891, Uptake and function of anthrax toxins

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.C.42.1.1, the channel-forming bacillus anthracis protective antigen (bapa) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Protective antigen1 Publication
Short name:
PA1 Publication
Alternative name(s):
Anthrax toxins translocating proteinCurated
PA-831 Publication
Short name:
PA831 Publication
Cleaved into the following 2 chains:
Protective antigen PA-20Curated
Short name:
PA-202 Publications
Short name:
PA202 Publications
Protective antigen PA-63Curated
Short name:
PA-632 Publications
Short name:
PA632 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:pagA
Synonyms:pag
Ordered Locus Names:pXO1-110, BXA0164, GBAA_pXO1_0164
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniPlasmid pXO1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBacillus anthracis
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1392 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000594 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Plasmid pXO1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei331 – 342Beta strandedCombined sources2 PublicationsAdd BLAST12
Transmembranei345 – 354Beta strandedCombined sources2 Publications10

Keywords - Cellular componenti

Host cell membrane, Host endosome, Host membrane, Membrane, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi193 – 196RKKR → SNSS or SNKE: Abolished cleavage by FURIN and abolished toxin activity. 1 Publication4
Mutagenesisi193R → A: Reduced cleavage by FURIN and reduced toxin activity. 1 Publication1
Mutagenesisi194 – 196KKR → EGG: Abolished cleavage by FURIN and abolished toxin activity. 1 Publication3
Mutagenesisi194 – 195KK → AA: Does not affect cleavage by FURIN and does not affect toxin activity. 1 Publication2
Mutagenesisi207R → A: Abolished interaction with LF. 1 Publication1
Mutagenesisi213P → A: Decrease in the ability to bind to LF and partially toxic at high concentrations. 1 Publication1
Mutagenesisi216L → A: Decrease in the ability to bind to LF and partially toxic at high concentrations. 1 Publication1
Mutagenesisi229R → S: Abolished interaction with LF. 1 Publication1
Mutagenesisi231F → A: Loss of ability to bind to LF and completely non-toxic. 1 Publication1
Mutagenesisi231F → S: Does not affect significantly interaction with LF, while it impairs tranlocation of LF. 1 Publication1
Mutagenesisi232L → A: Loss of ability to bind to LF and completely non-toxic. 1 Publication1
Mutagenesisi234P → A: Loss of ability to bind to LF and completely non-toxic. 1 Publication1
Mutagenesisi234P → S: Does not affect significantly interaction with LF. 1 Publication1
Mutagenesisi236I → A: Loss of ability to bind to LF and completely non-toxic. 1 Publication1
Mutagenesisi236I → S: Abolished interaction with LF. 1 Publication1
Mutagenesisi239I → A: Decrease in the ability to bind to LF and partially toxic at high concentrations. 1 Publication1
Mutagenesisi240H → A: Abolished interaction with LF. 1 Publication1
Mutagenesisi255W → A: No effect on LF-binding ability and as toxic as the wild-type. 1 Publication1
Mutagenesisi265F → A: No effect on LF-binding ability and as toxic as the wild-type. 1 Publication1
Mutagenesisi265F → S: Impaired translocation of LF. 1 Publication1
Mutagenesisi289P → A: Reduced toxicity in combination with lethal factor. Decreased membrane insertion and translocation of LF. 1 Publication1
Mutagenesisi342 – 344FFD → AAA: Decrease in toxicity probably due to slow translocation of LF. 1 Publication3
Mutagenesisi342 – 343Missing : Loss of toxicity probably due to loss of capability to translocate LF. 1 Publication2
Mutagenesisi342F → C: Loss of toxicity probably due to loss of capability to translocate LF. 1 Publication1
Mutagenesisi344D → A: Decrease in toxicity probably due to slow translocation of LF. 1 Publication1
Mutagenesisi375W → A: Loss of toxicity probably due to faulty membrane insertion or translocation of LF/EF into the cytosol. 1 Publication1
Mutagenesisi379M → A: No effect. 1 Publication1
Mutagenesisi381L → A: Loss of toxicity probably due to faulty membrane insertion or translocation of LF/EF into the cytosol. 1 Publication1
Mutagenesisi393I → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi409T → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi411S → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi422T → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi426K → A or D: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications1
Mutagenesisi428N → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi440Y → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi451N → C: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 1 Publication1
Mutagenesisi454D → A or K: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications1
Mutagenesisi456F → A: Loss of capability to undergo conformational changes that lead to pore formation and translocation. 2 Publications1
Mutagenesisi456F → C: Abolished ability for mediate LF and EF protein translocation. 1 Publication1
Mutagenesisi512Q → A: Loss of heptamerization capability. 1 Publication1
Mutagenesisi541D → A: Loss of heptamerization capability. 1 Publication1
Mutagenesisi543L → A: Decrease in heptamerization capability. 1 Publication1
Mutagenesisi581F → A: Loss of toxicity due to defective oligomerization. 1 Publication1
Mutagenesisi583F → A: Decrease in toxicity due to defective oligomerization. 1 Publication1
Mutagenesisi591I → A: Loss of toxicity due to defective oligomerization. 1 Publication1
Mutagenesisi595L → A: Loss of toxicity due to defective oligomerization. 1 Publication1
Mutagenesisi603I → A: Loss of toxicity due to defective oligomerization. 1 Publication1
Mutagenesisi621R → A: No effect. 1 Publication1
Mutagenesisi686N → A: Decrease in toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi708K → A: No effect on toxicity. 1 Publication1
Mutagenesisi709K → A: Slight decrease in toxicity. 1 Publication1
Mutagenesisi710Y → A: Great decrease in toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi711N → A: Loss of toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi712D → A: Loss of toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi713K → A: No effect on toxicity. 1 Publication1
Mutagenesisi714L → A: No effect on toxicity. 1 Publication1
Mutagenesisi715P → A: Great decrease in toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi716L → A: Decrease in toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi717Y → A: No effect on toxicity. 1 Publication1
Mutagenesisi718I → A: Decrease in toxicity due to decrease in cell binding. 1 Publication1
Mutagenesisi719S → A: No effect on toxicity. 1 Publication1
Mutagenesisi720N → A: No effect on toxicity. 1 Publication1
Mutagenesisi721P → A: No effect on toxicity. 1 Publication1
Mutagenesisi722N → A: No effect on toxicity. 1 Publication1

Miscellaneous databases

Pathogen-Host Interaction database

More...
PHI-basei
PHI:4090

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5352

Drug and drug target database

More...
DrugBanki
DB09057, Anthrax immune globulin human
DB08902, Raxibacumab

DrugCentral

More...
DrugCentrali
P13423

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 291 PublicationAdd BLAST29
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002199630 – 764Protective antigenAdd BLAST735
ChainiPRO_000002199730 – 196Protective antigen PA-202 PublicationsAdd BLAST167
ChainiPRO_0000021998197 – 764Protective antigen PA-632 PublicationsAdd BLAST568

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Proteolytic activation by FURIN cleaves the protein in two parts, PA-20 and PA-63; the latter is the mature protein (PubMed:1644824, PubMed:1438214, PubMed:8051159, PubMed:11207581). The cleavage occurs at the cell surface and probably in the serum of infected animals as well; both native and cleaved PA are able to bind to the cell receptor (PubMed:8051159, PubMed:11207581). The release of PA-20 from the remaining receptor-bound PA-63 exposes the binding site for EF and LF, and promotes oligomerization and internalization of the protein (PubMed:8051159, PubMed:11207581).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei196 – 197Cleavage; by FURIN3 Publications2
Sitei343 – 344Cleavage; by chymotrypsin; required for translocation of LF and EF1 Publication2

Keywords - PTMi

Cleavage on pair of basic residues

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with host ANTXR1 and ANTXR2.

4 Publications

Homooligomer; homooligomerizes to form homoheptamers (PA-637) or homooctamers (PA-638) (PubMed:10085027, PubMed:16051798, PubMed:19627991, PubMed:20433851, PubMed:25778700, PubMed:32810181). PA-637 or PA-638 form ring-shaped oligomers that are in a pre-pore conformation, which do not penetrate the host membrane (PubMed:19627991, PubMed:20433851, PubMed:32810181). PA-638 displays an enhanced stability, suggesting that this form circulates in the blood to reach and exert toxicity even in distant tissues (PubMed:20433851).

Interacts with lethal factor (LF) and edema factor (EF); can bind LF and EF simultaneously and interaction takes place following homooligomerization on the host cell membrane (PubMed:10085027, PubMed:12117959, PubMed:15313199, PubMed:21037566, PubMed:32047164, PubMed:32810181, PubMed:32521227). PA-637 homoheptamer interacts with three molecules of LF to form the PA7LF3 complex, in which the relative position of the N-terminal alpha-helices in the three LFs determines which factor is translocated first (PubMed:32810181).

11 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-29841N

Protein interaction database and analysis system

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IntActi
P13423, 16 interactors

Molecular INTeraction database

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MINTi
P13423

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P13423

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1764
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P13423

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P13423

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini43 – 179PA14PROSITE-ProRule annotationAdd BLAST137

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni30 – 287Domain 1, calcium-binding; LF and EF binding sites1 PublicationAdd BLAST258
Regioni176 – 214DisorderedSequence analysisAdd BLAST39
Regioni231 – 239Alpha-clamp1 Publication9
Regioni288 – 516Domain 2, membrane insertion and heptamerization1 PublicationAdd BLAST229
Regioni302 – 333DisorderedSequence analysisAdd BLAST32
Regioni517 – 624Domain 3, heptamerization1 PublicationAdd BLAST108
Regioni625 – 764Domain 4, binding to the receptor1 PublicationAdd BLAST140

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi302 – 331Polar residuesSequence analysisAdd BLAST30

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The molecule is folded into four functional domains (PubMed:1651334, PubMed:9039918). Each domain is required for a particular step in the toxicity process (PubMed:1651334). Domain 1 contains two calcium ions and the proteolytic activation site (PubMed:1651334). Cleavage of the PA monomer releases the subdomain 1a, which is the N-terminal fragment of 20-kDa (PA-20) (PubMed:8051159, PubMed:11207581, PubMed:9039918). The subdomain 1b is part of the remaining 63-kDa fragment (PA-63) and contains the binding sites for LP and EF (PubMed:8051159, PubMed:11207581, PubMed:9039918). Domain 2 is a beta-barrel core containing a large flexible loop that has been implicated in membrane insertion and pore formation (PubMed:1651334, PubMed:11356563, PubMed:9039918). There is a chymotrypsin cleavage site in this loop that is required for toxicity (PubMed:1512256, PubMed:7961869, PubMed:9039918). Domain 3 has a hydrophobic patch thought to be involved in protein-protein interactions (PubMed:1651334, PubMed:11222612, PubMed:9039918). Domain 4 appears to be a separate domain and shows limited contact with the other three domains: it would swing out of the way during membrane insertion (PubMed:1651334, PubMed:10085028, PubMed:12771151, PubMed:9039918). It is required for binding to the receptor; the small loop is involved in receptor recognition (PubMed:1651334, PubMed:10085028, PubMed:12771151, PubMed:9039918).10 Publications
Phe-456 residue forms the phi-clamp in the pore and catalyzes protein translocation via a charge-state-dependent Brownian ratchet (PubMed:16051798, PubMed:25778700). During conversion of the heptameric pre-pore precursor to the pore, the seven Phe-427 residues converge within the lumen to generate the narrowest point in the channel lumen (6 Angstroms in width) (PubMed:16051798, PubMed:25778700). To pass through this hydrophobic restriction, substrate proteins LF and EF need to be unfolded prior to translocation (PubMed:25778700).2 Publications
The alpha-clamp consists in an amphipathic cleft between two adjacent PA protomers, which assists the unfolding of substrate proteins LF and EF (PubMed:21037566, PubMed:32047164, PubMed:32521227). The alpha-clamp binds non-specifically to alpha-helices of substrate proteins LF and EF (PubMed:21037566, PubMed:32047164, PubMed:32521227).3 Publications

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the bacterial binary toxin family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_015269_0_0_9

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.120.240, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003896, Bacterial_exotoxin_B
IPR035331, Binary_toxB_3
IPR037524, PA14/GLEYA
IPR011658, PA14_dom
IPR035088, PA_Ca-bd
IPR027439, PA_heptamer_dom
IPR037149, PA_heptamer_dom_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF03495, Binary_toxB, 1 hit
PF17475, Binary_toxB_2, 1 hit
PF17476, Binary_toxB_3, 1 hit
PF07691, PA14, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01391, BINARYTOXINB

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00758, PA14, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51820, PA14, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P13423-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKRKVLIPL MALSTILVSS TGNLEVIQAE VKQENRLLNE SESSSQGLLG
60 70 80 90 100
YYFSDLNFQA PMVVTSSTTG DLSIPSSELE NIPSENQYFQ SAIWSGFIKV
110 120 130 140 150
KKSDEYTFAT SADNHVTMWV DDQEVINKAS NSNKIRLEKG RLYQIKIQYQ
160 170 180 190 200
RENPTEKGLD FKLYWTDSQN KKEVISSDNL QLPELKQKSS NSRKKRSTSA
210 220 230 240 250
GPTVPDRDND GIPDSLEVEG YTVDVKNKRT FLSPWISNIH EKKGLTKYKS
260 270 280 290 300
SPEKWSTASD PYSDFEKVTG RIDKNVSPEA RHPLVAAYPI VHVDMENIIL
310 320 330 340 350
SKNEDQSTQN TDSQTRTISK NTSTSRTHTS EVHGNAEVHA SFFDIGGSVS
360 370 380 390 400
AGFSNSNSST VAIDHSLSLA GERTWAETMG LNTADTARLN ANIRYVNTGT
410 420 430 440 450
APIYNVLPTT SLVLGKNQTL ATIKAKENQL SQILAPNNYY PSKNLAPIAL
460 470 480 490 500
NAQDDFSSTP ITMNYNQFLE LEKTKQLRLD TDQVYGNIAT YNFENGRVRV
510 520 530 540 550
DTGSNWSEVL PQIQETTARI IFNGKDLNLV ERRIAAVNPS DPLETTKPDM
560 570 580 590 600
TLKEALKIAF GFNEPNGNLQ YQGKDITEFD FNFDQQTSQN IKNQLAELNA
610 620 630 640 650
TNIYTVLDKI KLNAKMNILI RDKRFHYDRN NIAVGADESV VKEAHREVIN
660 670 680 690 700
SSTEGLLLNI DKDIRKILSG YIVEIEDTEG LKEVINDRYD MLNISSLRQD
710 720 730 740 750
GKTFIDFKKY NDKLPLYISN PNYKVNVYAV TKENTIINPS ENGDTSTNGI
760
KKILIFSKKG YEIG
Length:764
Mass (Da):85,811
Last modified:October 18, 2001 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3AE1EFBF48FAA03F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti314Q → E in AAA22637 (PubMed:3148491).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti295M → I in strain: PAI. 1 Publication1
Natural varianti392N → D in strain: PAI. 1 Publication1
Natural varianti560F → L in Sverdlovsk sample. 1
Natural varianti565P → S in strain: BA1024. 1 Publication1
Natural varianti600A → V in strain: BA1024, V770-NP1-R, Carbosap and Ferrara. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M22589 Genomic DNA Translation: AAA22637.1
AF306778 Genomic DNA Translation: AAG24446.1
AF306779 Genomic DNA Translation: AAG24447.1
AF306780 Genomic DNA Translation: AAG24448.1
AF306781 Genomic DNA Translation: AAG24449.1
AF306782 Genomic DNA Translation: AAG24450.1
AF306783 Genomic DNA Translation: AAG24451.1
AF268967 Genomic DNA Translation: AAF86457.1
AF065404 Genomic DNA Translation: AAD32414.1
AE011190 Genomic DNA Translation: AAM26109.1
AE017336 Genomic DNA Translation: AAT28905.2
AJ413936 Genomic DNA Translation: CAC93934.1
AJ413937 Genomic DNA Translation: CAC93935.1
AB125961 Genomic DNA Translation: BAD14937.1

Protein sequence database of the Protein Information Resource

More...
PIRi
I39934

NCBI Reference Sequences

More...
RefSeqi
NP_052806.1, NC_001496.1
WP_000746486.1, NZ_SDEF01000130.1
WP_000746487.1, NZ_QAEM01000007.1
WP_000746488.1, NZ_VTZH01000015.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAT28905; AAT28905; GBAA_pXO1_0164

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
45025512

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bar:GBAA_pXO1_0164

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22589 Genomic DNA Translation: AAA22637.1
AF306778 Genomic DNA Translation: AAG24446.1
AF306779 Genomic DNA Translation: AAG24447.1
AF306780 Genomic DNA Translation: AAG24448.1
AF306781 Genomic DNA Translation: AAG24449.1
AF306782 Genomic DNA Translation: AAG24450.1
AF306783 Genomic DNA Translation: AAG24451.1
AF268967 Genomic DNA Translation: AAF86457.1
AF065404 Genomic DNA Translation: AAD32414.1
AE011190 Genomic DNA Translation: AAM26109.1
AE017336 Genomic DNA Translation: AAT28905.2
AJ413936 Genomic DNA Translation: CAC93934.1
AJ413937 Genomic DNA Translation: CAC93935.1
AB125961 Genomic DNA Translation: BAD14937.1
PIRiI39934
RefSeqiNP_052806.1, NC_001496.1
WP_000746486.1, NZ_SDEF01000130.1
WP_000746487.1, NZ_QAEM01000007.1
WP_000746488.1, NZ_VTZH01000015.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ACCX-ray2.10A30-764[»]
1T6BX-ray2.50X30-764[»]
1TX5model-C30-764[»]
1TZNX-ray4.30A/B/C/D/E/F/G/H/I/J/K/L/M/O203-764[»]
1TZOX-ray3.60A/B/C/D/E/F/G/H/I/J/K/L/M/O203-764[»]
1V36model-A/B/C/D/E/F/G197-764[»]
3ETBX-ray3.80J/K/L/M621-764[»]
3INOX-ray1.95A/B624-764[»]
3J9Celectron microscopy2.90A203-764[»]
3KWVX-ray3.10A/B/D/E197-764[»]
3MHZX-ray1.70A30-764[»]
3Q8AX-ray3.13A30-764[»]
3Q8BX-ray2.00A30-764[»]
3Q8CX-ray2.85A30-764[»]
3Q8EX-ray2.10A30-764[»]
3Q8FX-ray2.10A30-764[»]
3TEWX-ray1.45A30-764[»]
3TEXX-ray1.70A30-764[»]
3TEYX-ray2.12A30-764[»]
3TEZX-ray1.83A30-764[»]
4EE2X-ray1.91A30-764[»]
4H2AX-ray1.62A30-764[»]
4NAMX-ray1.70A30-764[»]
5FR3X-ray1.94A43-764[»]
6PSNelectron microscopy4.60A/B/C/D/E/F/G197-764[»]
6UJIX-ray5.50A/B/C/D/E/F/G/H/I/J/K/L/M/N197-764[»]
6UZBelectron microscopy3.20A/B/C/D/E/F/G30-764[»]
6UZDelectron microscopy3.40A/B/C/D/E/F/G30-764[»]
6UZEelectron microscopy3.40A/B/C/D/E/F/G30-764[»]
6VRAelectron microscopy3.30A/B/C/D/E/F/G/H33-764[»]
6WJJelectron microscopy3.80A/B/C/D/E/F/G/H33-764[»]
6ZXJelectron microscopy3.50A/B/C/D/E/F/G29-764[»]
6ZXKelectron microscopy3.80A/B/C/D/E/F/G29-764[»]
6ZXLelectron microscopy4.20A/B/C/D/E/F/G29-764[»]
SMRiP13423
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-29841N
IntActiP13423, 16 interactors
MINTiP13423

Chemistry databases

BindingDBiP13423
ChEMBLiCHEMBL5352
DrugBankiDB09057, Anthrax immune globulin human
DB08902, Raxibacumab
DrugCentraliP13423

Protein family/group databases

TCDBi1.C.42.1.1, the channel-forming bacillus anthracis protective antigen (bapa) family

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P13423, 35 sequenced antibodies

Genome annotation databases

EnsemblBacteriaiAAT28905; AAT28905; GBAA_pXO1_0164
GeneIDi45025512
KEGGibar:GBAA_pXO1_0164

Phylogenomic databases

HOGENOMiCLU_015269_0_0_9

Enzyme and pathway databases

ReactomeiR-HSA-5210891, Uptake and function of anthrax toxins

Miscellaneous databases

EvolutionaryTraceiP13423
PHI-baseiPHI:4090

Protein Ontology

More...
PROi
PR:P13423

Family and domain databases

Gene3Di2.60.120.240, 1 hit
InterProiView protein in InterPro
IPR003896, Bacterial_exotoxin_B
IPR035331, Binary_toxB_3
IPR037524, PA14/GLEYA
IPR011658, PA14_dom
IPR035088, PA_Ca-bd
IPR027439, PA_heptamer_dom
IPR037149, PA_heptamer_dom_sf
PfamiView protein in Pfam
PF03495, Binary_toxB, 1 hit
PF17475, Binary_toxB_2, 1 hit
PF17476, Binary_toxB_3, 1 hit
PF07691, PA14, 1 hit
PRINTSiPR01391, BINARYTOXINB
SMARTiView protein in SMART
SM00758, PA14, 1 hit
PROSITEiView protein in PROSITE
PS51820, PA14, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPAG_BACAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P13423
Secondary accession number(s): Q937W2
, Q937W3, Q9F5R7, Q9KH69, Q9RQU2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 18, 2001
Last modified: June 2, 2021
This is version 197 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Plasmid, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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